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Q03526

- ITK_MOUSE

UniProt

Q03526 - ITK_MOUSE

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Protein

Tyrosine-protein kinase ITK/TSK

Gene

Itk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi138 – 1381ZincBy similarity
Metal bindingi139 – 1391ZincBy similarity
Metal bindingi149 – 1491ZincBy similarity
Binding sitei396 – 3961ATPPROSITE-ProRule annotation
Active sitei487 – 4871Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri119 – 15537Btk-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi374 – 3829ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of phospholipase C activity Source: UniProtKB
  2. adaptive immune response Source: UniProtKB
  3. cytokine production Source: UniProtKB
  4. interferon-gamma production Source: MGI
  5. interleukin-4 production Source: MGI
  6. intracellular signal transduction Source: InterPro
  7. NK T cell differentiation Source: MGI
  8. peptidyl-tyrosine phosphorylation Source: GOC
  9. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_188202. FCERI mediated Ca+2 mobilization.
REACT_225768. Generation of second messenger molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase ITK/TSK (EC:2.7.10.2)
Alternative name(s):
IL-2-inducible T-cell kinase
Kinase EMT
Kinase TLK
T-cell-specific kinase
Gene namesi
Name:Itk
Synonyms:Emt, Tlk, Tsk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:96621. Itk.

Subcellular locationi

Cytoplasm
Note: Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation.By similarity

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice display decreased mature thymocytes and elicit profound defect in CD4+ and CD8+ T-cell development. Additionally, they show a strong decrease of cytokine production in response to TCR receptor stimulation.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625Tyrosine-protein kinase ITK/TSKPRO_0000088107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphotyrosine; by autocatalysisBy similarity
Modified residuei517 – 5171Phosphotyrosine; by LCKBy similarity
Modified residuei570 – 5701PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated at Tyr-517 in the activation loop of the kinase domain by LCK. Subsequent autophosphorylation at Tyr-186 leads to the kinase activation. The autophosphorylated Tyr-186 lies within the substrate binding sequence of the SH3 domain (By similarity).By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ03526.

PTM databases

PhosphoSiteiQ03526.

Expressioni

Tissue specificityi

Is detected in the thymus, lymph node and very faintly in the spleen, but is not detected in the liver, lung, kidney, heart, brain, intestine or testis. Expressed in T-lymphocytes and mast cells. It may also be expressed in natural killer cells.

Developmental stagei

Is present in the fetal thymus as early as day 14 of gestation. The levels are 5- to 10-fold higher in thymocytes than in peripheral T-cells, and increase in the thymus during development from neonate to adult.

Inductioni

Through a myriad of surface receptors including the TCR/CD3 signaling complex, coreceptors, or chemokine receptors.

Gene expression databases

BgeeiQ03526.
CleanExiMM_ITK.
ExpressionAtlasiQ03526. baseline and differential.
GenevestigatoriQ03526.

Interactioni

Subunit structurei

Homooligomerizes; this association negatively regulates kinase activity. Interacts with PPIA/CYPA; this interaction regulates TCR signal strength via a proline-directed conformational switch in ITK. Interacts with THEMIS (By similarity). Interacts with FASLG. Interacts with VAV1; this interaction is important for VAV1 localization and TCR-induced actin polarization.By similarity2 Publications

Protein-protein interaction databases

BioGridi200840. 5 interactions.
DIPiDIP-29283N.
IntActiQ03526. 4 interactions.
MINTiMINT-84965.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1803
Beta strandi181 – 1866
Beta strandi192 – 1954
Beta strandi200 – 2023
Beta strandi203 – 2053
Beta strandi211 – 2144
Beta strandi215 – 2184
Beta strandi220 – 2223
Beta strandi224 – 2263
Beta strandi229 – 2346
Helixi240 – 2423
Beta strandi243 – 2464
Beta strandi248 – 2503
Helixi252 – 26211
Beta strandi268 – 2725
Turni275 – 2773
Beta strandi279 – 2857
Beta strandi290 – 2923
Beta strandi294 – 3029
Beta strandi305 – 3073
Beta strandi310 – 3134
Beta strandi318 – 3203
Helixi321 – 33010
Beta strandi335 – 3373
Beta strandi338 – 3425

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWJNMR-A160-236[»]
1LUINMR-A238-344[»]
1LUKNMR-A238-344[»]
1LUMNMR-A238-344[»]
1LUNNMR-A238-344[»]
2ETZNMR-A238-344[»]
2EU0NMR-A238-344[»]
2K79NMR-A177-237[»]
B238-344[»]
2K7ANMR-A177-237[»]
B238-344[»]
2RN8NMR-A177-238[»]
2RNANMR-A177-238[»]
3S9KX-ray2.35A236-344[»]
ProteinModelPortaliQ03526.
SMRiQ03526. Positions 5-623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03526.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 117114PHPROSITE-ProRule annotationAdd
BLAST
Domaini177 – 23761SH3PROSITE-ProRule annotationAdd
BLAST
Domaini245 – 34399SH2PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 620253Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The N-terminal PH domain allows ITK to be recruited to the plasma membrane by an activated PI3 kinase. This domain contains also a proline-rich region (PRR). The adjoining domain is a SH3 domain, which binds to PRR (from itself or from other proteins). Next, a SH2 domain is required for binding tyrosine-phosphorylated substrates. In the C-terminal region, the kinase domain is required for tyrosine phosphorylation (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri119 – 15537Btk-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiQ03526.
KOiK07363.
OMAiRRNEEYC.
PhylomeDBiQ03526.
TreeFamiTF351634.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamiPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTiSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03526-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNFILLEEQ LIKKSQQKRR TSPSNFKVRF FVLTKASLAY FEDRHGKKRT
60 70 80 90 100
LKGSIELSRI KCVEIVKSDI SIPCHYKYPF QTLVYLQVVH DNYLLYVFAP
110 120 130 140 150
DCESRQRWVL TLKEETRNNN SLVSKYHPNF WMDGRWRCCS QLEKPAVGCA
160 170 180 190 200
PYDPSKNASK KPLPPTPEDN RRSFQEPEET LVIALYDYQT NDPQELALRC
210 220 230 240 250
DEEYYLLDSS EIHWWRVQDK NGHEGYAPSS YLVEKSPNNL ETYEWYNKSI
260 270 280 290 300
SRDKAEKLLL DTGKEGAFMV RDSRTPGTYT VSVFTKAIIS ENPCIKHYHI
310 320 330 340 350
KETNDSPKRY YVAEKYVFDS IPLLIQYHQY NGGGLVTRLR YPVCSWRQKA
360 370 380 390 400
PVTAGLRYGK WVIQPSELTF VQEIGSGQFG LVHLGYWLNK DKVAIKTIQE
410 420 430 440 450
GAMSEEDFIE EAEVMMKLSH PKLVQLYGVC LEQAPICLVF EFMEHGCLSD
460 470 480 490 500
YLRSQRGLFA AETLLGMCLD VCEGMAYLEK ACVIHRDLAA RNCLVGENQV
510 520 530 540 550
IKVSDFGMTR FVLDDQYTSS TGTKFPVKWA SPEVFSFSRY SSKSDVWSFG
560 570 580 590 600
VLMWEVFSEG KIPYENRSNS EVVEDISTGF RLYKPRLASC HVYQIMNHCW
610 620
KEKPEDRPPF SQLLSQLAEI AEAGL
Length:625
Mass (Da):72,292
Last modified:February 1, 1995 - v1
Checksum:iF7A4A18A8A1AADDC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 876Missing(PubMed:8421704)Curated
Sequence conflicti82 – 876Missing(PubMed:8476425)Curated
Sequence conflicti82 – 876Missing1 PublicationCurated
Sequence conflicti535 – 5351F → S in L10628. (PubMed:8476425)Curated
Sequence conflicti540 – 5401Y → C in L10628. (PubMed:8476425)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00619 mRNA. Translation: AAA39337.1.
L05631 mRNA. Translation: AAA40518.1.
L10628 mRNA. No translation available.
D14042 mRNA. Translation: BAA03129.1.
CCDSiCCDS70169.1.
PIRiA43030.
RefSeqiNP_001268894.1. NM_001281965.1.
NP_001268895.1. NM_001281966.1.
NP_001268897.1. NM_001281968.1.
NP_034713.2. NM_010583.3.
UniGeneiMm.339927.

Genome annotation databases

EnsembliENSMUST00000109237; ENSMUSP00000104860; ENSMUSG00000020395.
GeneIDi16428.
KEGGimmu:16428.
UCSCiuc011xtn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00619 mRNA. Translation: AAA39337.1 .
L05631 mRNA. Translation: AAA40518.1 .
L10628 mRNA. No translation available.
D14042 mRNA. Translation: BAA03129.1 .
CCDSi CCDS70169.1.
PIRi A43030.
RefSeqi NP_001268894.1. NM_001281965.1.
NP_001268895.1. NM_001281966.1.
NP_001268897.1. NM_001281968.1.
NP_034713.2. NM_010583.3.
UniGenei Mm.339927.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AWJ NMR - A 160-236 [» ]
1LUI NMR - A 238-344 [» ]
1LUK NMR - A 238-344 [» ]
1LUM NMR - A 238-344 [» ]
1LUN NMR - A 238-344 [» ]
2ETZ NMR - A 238-344 [» ]
2EU0 NMR - A 238-344 [» ]
2K79 NMR - A 177-237 [» ]
B 238-344 [» ]
2K7A NMR - A 177-237 [» ]
B 238-344 [» ]
2RN8 NMR - A 177-238 [» ]
2RNA NMR - A 177-238 [» ]
3S9K X-ray 2.35 A 236-344 [» ]
ProteinModelPortali Q03526.
SMRi Q03526. Positions 5-623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200840. 5 interactions.
DIPi DIP-29283N.
IntActi Q03526. 4 interactions.
MINTi MINT-84965.

PTM databases

PhosphoSitei Q03526.

Proteomic databases

PRIDEi Q03526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109237 ; ENSMUSP00000104860 ; ENSMUSG00000020395 .
GeneIDi 16428.
KEGGi mmu:16428.
UCSCi uc011xtn.1. mouse.

Organism-specific databases

CTDi 3702.
MGIi MGI:96621. Itk.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi Q03526.
KOi K07363.
OMAi RRNEEYC.
PhylomeDBi Q03526.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_225768. Generation of second messenger molecules.

Miscellaneous databases

EvolutionaryTracei Q03526.
NextBioi 289653.
PROi Q03526.
SOURCEi Search...

Gene expression databases

Bgeei Q03526.
CleanExi MM_ITK.
ExpressionAtlasi Q03526. baseline and differential.
Genevestigatori Q03526.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view ]
Pfami PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTi SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "itk, a T-cell-specific tyrosine kinase gene inducible by interleukin 2."
    Siliciano J.D., Morrow T.A., Desiderio S.V.
    Proc. Natl. Acad. Sci. U.S.A. 89:11194-11198(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymocyte.
  2. "Developmental regulation of a murine T-cell-specific tyrosine kinase gene, Tsk."
    Heyeck S.D., Berg L.J.
    Proc. Natl. Acad. Sci. U.S.A. 90:669-673(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymocyte.
  3. "Structure and expression of novel protein-tyrosine kinases, Emb and Emt, in hematopoietic cells."
    Yamada N., Kawakami Y., Kimura H., Fukamachi H., Baier G., Altman A., Kato T., Inagaki Y., Kawakami T.
    Biochem. Biophys. Res. Commun. 192:231-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CBA/J.
    Tissue: Mast cell.
  4. Ogata M., Sawada M., Fujiwara H., Hamaoka T.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk."
    Liao X.C., Littman D.R.
    Immunity 3:757-769(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Themis controls thymocyte selection through regulation of T cell antigen receptor-mediated signaling."
    Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C., Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J., Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J.
    Nat. Immunol. 10:848-856(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THEMIS.
  7. "Regulatory intramolecular association in a tyrosine kinase of the Tec family."
    Andreotti A.H., Bunnell S.C., Feng S., Berg L.J., Schreiber S.L.
    Nature 385:93-97(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 160-236.
  8. "CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line."
    August A., Gibson S., Kawakami Y., Kawakami T., Mills G.B., Dupont B.
    Proc. Natl. Acad. Sci. U.S.A. 91:9347-9351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "CD2 signaling in T cells involves tyrosine phosphorylation and activation of the Tec family kinase, EMT/ITK/TSK."
    King P.D., Sadra A., Han A., Liu X.-R., Sunder-Plassmann R., Reinherz E.L., Dupont B.
    Int. Immunol. 8:1707-1714(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Emt/Itk associates with activated TCR complexes: role of the pleckstrin homology domain."
    Ching K.A., Kawakami Y., Kawakami T., Tsoukas C.D.
    J. Immunol. 163:6006-6013(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "Requirement for Tec kinases Rlk and Itk in T cell receptor signaling and immunity."
    Schaeffer E.M., Debnath J., Yap G., McVicar D., Liao X.C., Littman D.R., Sher A., Varmus H.E., Lenardo M.J., Schwartzberg P.L.
    Science 284:638-641(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  12. "Altered development of CD8+ T cell lineages in mice deficient for the Tec kinases Itk and Rlk."
    Broussard C., Fleischacker C., Horai R., Chetana M., Venegas A.M., Sharp L.L., Hedrick S.M., Fowlkes B.J., Schwartzberg P.L.
    Immunity 25:93-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "Disrupting the intermolecular self-association of Itk enhances T cell signaling."
    Min L., Wu W., Joseph R.E., Fulton D.B., Berg L., Andreotti A.H.
    J. Immunol. 184:4228-4235(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  14. "Interleukin-2-inducible T cell kinase (Itk) network edge dependence for the maturation of iNKT cell."
    Qi Q., Xia M., Bai Y., Yu S., Cantorna M., August A.
    J. Biol. Chem. 286:138-146(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INVARIANT NKT CELL MATURATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiITK_MOUSE
AccessioniPrimary (citable) accession number: Q03526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3